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Volumn 14, Issue 1, 2010, Pages 30-36

Designs and applications of fluorescent protein-based biosensors

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; CALMODULIN; ENHANCED GREEN FLUORESCENT PROTEIN; G PROTEIN COUPLED RECEPTOR; GREEN FLUORESCENT PROTEIN; YELLOW FLUORESCENT PROTEIN;

EID: 75149112222     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2009.09.033     Document Type: Review
Times cited : (156)

References (47)
  • 1
    • 75149177129 scopus 로고    scopus 로고
    • Advances in engineering of monomeric fluorescent proteins and photoactivatable proteins with red emission
    • Piatkevich K.D., and Verkhusha VV. Advances in engineering of monomeric fluorescent proteins and photoactivatable proteins with red emission. Curr Opin Chem Biol 14 (2010) 23-29
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 23-29
    • Piatkevich, K.D.1    Verkhusha VV2
  • 2
    • 68049093089 scopus 로고    scopus 로고
    • Fluorescent-protein-based biosensors: modulation of energy transfer as a design principle
    • Campbell R.E. Fluorescent-protein-based biosensors: modulation of energy transfer as a design principle. Anal Chem 81 (2009) 5972-5979
    • (2009) Anal Chem , vol.81 , pp. 5972-5979
    • Campbell, R.E.1
  • 4
    • 50249098131 scopus 로고    scopus 로고
    • Fluorescence proteins, live-cell imaging, and mechanobiology: seeing is believing
    • A thorough review that covers the available FP variants and microscopy techniques for live-cell imaging.
    • Wang Y.X., Shyy J.Y.J., and Chien S. Fluorescence proteins, live-cell imaging, and mechanobiology: seeing is believing. Annu Rev Biomed Eng 10 (2008) 1-38. A thorough review that covers the available FP variants and microscopy techniques for live-cell imaging.
    • (2008) Annu Rev Biomed Eng , vol.10 , pp. 1-38
    • Wang, Y.X.1    Shyy, J.Y.J.2    Chien, S.3
  • 5
    • 59749091428 scopus 로고    scopus 로고
    • Real-time monitoring of human enterovirus (HEV)-infected cells and anti-HEV 3C protease potency by fluorescence resonance energy transfer
    • An elegant study showing HEV 3C protease FRET-based biosensor being used to establish a stable cell line which in turn is used to assay different viral serotypes and test them for their inhibition susceptibility in live cells.
    • Tsai M.T., Cheng Y.H., Liu Y.N., Liao N.C., Lu W.W., and Kung S.H. Real-time monitoring of human enterovirus (HEV)-infected cells and anti-HEV 3C protease potency by fluorescence resonance energy transfer. Antimicrob Agents Chemother 53 (2009) 748-755. An elegant study showing HEV 3C protease FRET-based biosensor being used to establish a stable cell line which in turn is used to assay different viral serotypes and test them for their inhibition susceptibility in live cells.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 748-755
    • Tsai, M.T.1    Cheng, Y.H.2    Liu, Y.N.3    Liao, N.C.4    Lu, W.W.5    Kung, S.H.6
  • 6
    • 59749089747 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer-based assay for characterization of hepatitis C virus NS3-4A protease activity in live cells
    • Sabariegos R., Picazo F., Domingo B., Franco S., Martinez M.A., and Llopis J. Fluorescence resonance energy transfer-based assay for characterization of hepatitis C virus NS3-4A protease activity in live cells. Antimicrob Agents Chemother 53 (2009) 728-734
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 728-734
    • Sabariegos, R.1    Picazo, F.2    Domingo, B.3    Franco, S.4    Martinez, M.A.5    Llopis, J.6
  • 8
    • 70349124959 scopus 로고    scopus 로고
    • Fluorescent biosensors for real-time tracking of post-translational modification dynamics
    • Aye-Han N.-N., Qiang N., and Zhang J. Fluorescent biosensors for real-time tracking of post-translational modification dynamics. Curr Opin Chem Biol 13 (2009) 392-397
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 392-397
    • Aye-Han, N.-N.1    Qiang, N.2    Zhang, J.3
  • 9
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: a versatile superfamily for protein engineering
    • Dwyer M.A., and Hellinga H.W. Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr Opin Struct Biol 14 (2004) 495-504
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.W.2
  • 11
    • 40949111343 scopus 로고    scopus 로고
    • GLUT1 and GLUT9 as major contributors to glucose influx in HepG2 cells identified by a high sensitivity intramolecular FRET glucose sensor
    • Takanaga H., Chaudhuri B., and Frommer W.B. GLUT1 and GLUT9 as major contributors to glucose influx in HepG2 cells identified by a high sensitivity intramolecular FRET glucose sensor. Biochim Biophys Acta Biomembr 1778 (2008) 1091-1099
    • (2008) Biochim Biophys Acta Biomembr , vol.1778 , pp. 1091-1099
    • Takanaga, H.1    Chaudhuri, B.2    Frommer, W.B.3
  • 12
    • 36649019154 scopus 로고    scopus 로고
    • Design and application of highly responsive fluorescence resonance energy transfer biosensors for detection of sugar in living Saccharomyces cerevisiae cells
    • Ha J.S., Song J.J., Lee Y.M., Kim S.J., Sohn J.H., Shin C.S., and Lee S.G. Design and application of highly responsive fluorescence resonance energy transfer biosensors for detection of sugar in living Saccharomyces cerevisiae cells. Appl Environ Microbiol 73 (2007) 7408-7414
    • (2007) Appl Environ Microbiol , vol.73 , pp. 7408-7414
    • Ha, J.S.1    Song, J.J.2    Lee, Y.M.3    Kim, S.J.4    Sohn, J.H.5    Shin, C.S.6    Lee, S.G.7
  • 13
    • 41949134810 scopus 로고    scopus 로고
    • Optical measurement of synaptic glutamate spillover and reuptake by linker optimized glutamate-sensitive fluorescent reporters
    • Hires S.A., Zhu Y.L., and Tsien R.Y. Optical measurement of synaptic glutamate spillover and reuptake by linker optimized glutamate-sensitive fluorescent reporters. Proc Natl Acad Sci U S A 105 (2008) 4411-4416
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4411-4416
    • Hires, S.A.1    Zhu, Y.L.2    Tsien, R.Y.3
  • 14
    • 56249108340 scopus 로고    scopus 로고
    • Measuring calcium dynamics in living cells with genetically encodable calcium indicators
    • McCombs J.E., and Palmer A.E. Measuring calcium dynamics in living cells with genetically encodable calcium indicators. Methods 46 (2008) 152-159
    • (2008) Methods , vol.46 , pp. 152-159
    • McCombs, J.E.1    Palmer, A.E.2
  • 15
    • 44849120336 scopus 로고    scopus 로고
    • Genetically encoded calcium indicators
    • Mank M., and Griesbeck O. Genetically encoded calcium indicators. Chem Rev 108 (2008) 1550-1564
    • (2008) Chem Rev , vol.108 , pp. 1550-1564
    • Mank, M.1    Griesbeck, O.2
  • 16
    • 67650257938 scopus 로고    scopus 로고
    • Genetically encoded sensors to elucidate spatial distribution of cellular zinc
    • Dittmer P.J., Miranda J.G., Gorski J.A., and Palmer A.E. Genetically encoded sensors to elucidate spatial distribution of cellular zinc. J Biol Chem 284 (2009) 16289-16297
    • (2009) J Biol Chem , vol.284 , pp. 16289-16297
    • Dittmer, P.J.1    Miranda, J.G.2    Gorski, J.A.3    Palmer, A.E.4
  • 17
    • 57049115401 scopus 로고    scopus 로고
    • Real-time monitoring of cyclic nucleotide signaling in neurons using genetically encoded FRET probes
    • Vincent P., Gervasi N., and Zhang J. Real-time monitoring of cyclic nucleotide signaling in neurons using genetically encoded FRET probes. Brain Cell Biol 36 (2008) 3-17
    • (2008) Brain Cell Biol , vol.36 , pp. 3-17
    • Vincent, P.1    Gervasi, N.2    Zhang, J.3
  • 18
    • 58449123608 scopus 로고    scopus 로고
    • Studies on the role of the receptor protein motifs possibly involved in electrostatic interactions on the dopamine D-1 and D-2 receptor oligomerization
    • Lukasiewicz S., Faron-Gorecka A., Dobrucki J., Polit A., and Dziedzicka-Wasylewska M. Studies on the role of the receptor protein motifs possibly involved in electrostatic interactions on the dopamine D-1 and D-2 receptor oligomerization. FEBS J 276 (2009) 760-775
    • (2009) FEBS J , vol.276 , pp. 760-775
    • Lukasiewicz, S.1    Faron-Gorecka, A.2    Dobrucki, J.3    Polit, A.4    Dziedzicka-Wasylewska, M.5
  • 20
    • 67650494991 scopus 로고    scopus 로고
    • Optical measurement of mGluR1 conformational changes reveals fast activation, slow deactivation, and sensitization
    • An interesting employment of the FRET phenomenon to study the activation kinetics of mGluR1. The authors demonstrate that the changes in FRET correlate with activation of the receptor.
    • Marcaggi P., Mutoh H., Dimitrov D., Beato M., and Knopfel T. Optical measurement of mGluR1 conformational changes reveals fast activation, slow deactivation, and sensitization. Proc Natl Acad Sci U S A 106 (2009) 11388-11393. An interesting employment of the FRET phenomenon to study the activation kinetics of mGluR1. The authors demonstrate that the changes in FRET correlate with activation of the receptor.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 11388-11393
    • Marcaggi, P.1    Mutoh, H.2    Dimitrov, D.3    Beato, M.4    Knopfel, T.5
  • 23
    • 48249132926 scopus 로고    scopus 로고
    • Biomolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells
    • A comprehensive review that covers the BiFC technique, the practical aspects of BiFC experiments, and the kind of applications it is suitable for.
    • Kerppola T.K. Biomolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu Rev Biophys 37 (2008) 465-487. A comprehensive review that covers the BiFC technique, the practical aspects of BiFC experiments, and the kind of applications it is suitable for.
    • (2008) Annu Rev Biophys , vol.37 , pp. 465-487
    • Kerppola, T.K.1
  • 24
    • 37249010179 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementatlon: visualization of molecular interactions in living cells
    • Kerppola T.K. Bimolecular fluorescence complementatlon: visualization of molecular interactions in living cells. Methods Cell Biol 85 (2008) 431-470
    • (2008) Methods Cell Biol , vol.85 , pp. 431-470
    • Kerppola, T.K.1
  • 25
    • 55949121452 scopus 로고    scopus 로고
    • Different polycomb group CBX family proteins associate with distinct regions of chromatin using nonhomologous protein sequences
    • Vincenz C., and Kerppola T.K. Different polycomb group CBX family proteins associate with distinct regions of chromatin using nonhomologous protein sequences. Proc Natl Acad Sci U S A 105 (2008) 16572-16577
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 16572-16577
    • Vincenz, C.1    Kerppola, T.K.2
  • 26
    • 64049093748 scopus 로고    scopus 로고
    • Detection and characterization of influenza A virus PA-PB2 interaction through a bimolecular fluorescence complementation assay
    • Hemerka J.N., Wang D., Weng Y.J., Lu W.X., Kaushik R.S., Jin J., Harmon A.F., and Li F. Detection and characterization of influenza A virus PA-PB2 interaction through a bimolecular fluorescence complementation assay. J Virol 83 (2009) 3944-3955
    • (2009) J Virol , vol.83 , pp. 3944-3955
    • Hemerka, J.N.1    Wang, D.2    Weng, Y.J.3    Lu, W.X.4    Kaushik, R.S.5    Jin, J.6    Harmon, A.F.7    Li, F.8
  • 27
    • 64249110099 scopus 로고    scopus 로고
    • Simultaneous visualization of two protein complexes in a single plant cell using multicolor fluorescence complementation analysis
    • Kodama Y., and Wada M. Simultaneous visualization of two protein complexes in a single plant cell using multicolor fluorescence complementation analysis. Plant Mol Biol 70 (2009) 211-217
    • (2009) Plant Mol Biol , vol.70 , pp. 211-217
    • Kodama, Y.1    Wada, M.2
  • 28
    • 50449091328 scopus 로고    scopus 로고
    • Ligand-dependent oligomerization of dopamine D2 and adenosine A(2A) receptors in living neuronal cells
    • 2 GPCRs, and how they are affected by the presence of certain drugs.
    • 2 GPCRs, and how they are affected by the presence of certain drugs.
    • (2008) Mol Pharmacol , vol.74 , pp. 544-551
    • Vidi, P.A.1    Chemel, B.R.2    Hu, C.D.3    Watts, V.J.4
  • 29
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent proteins
    • Baird G.S., Zacharias D.A., and Tsien R.Y. Circular permutation and receptor insertion within green fluorescent proteins. Proc Natl Acad Sci U S A 96 (1999) 11241-11246
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 31
    • 35248833734 scopus 로고    scopus 로고
    • Metal-ion-dependent GFP emission in vivo by combining a circularly permutated green fluorescent protein with an engineered metal-ion-binding coiled-coil
    • Mizuno T., Murao K., Tanabe Y., Oda M., and Tanaka T. Metal-ion-dependent GFP emission in vivo by combining a circularly permutated green fluorescent protein with an engineered metal-ion-binding coiled-coil. J Am Chem Soc 129 (2007) 11378-11383
    • (2007) J Am Chem Soc , vol.129 , pp. 11378-11383
    • Mizuno, T.1    Murao, K.2    Tanabe, Y.3    Oda, M.4    Tanaka, T.5
  • 32
    • 38349099574 scopus 로고    scopus 로고
    • Differential patterning of cGMP in vascular smooth muscle cells revealed by single GFP-linked biosensors
    • Nausch L.W.M., Lecloux J., Bonev A.D., Nelson M.T., and Dostmann W.R. Differential patterning of cGMP in vascular smooth muscle cells revealed by single GFP-linked biosensors. Proc Natl Acad Sci U S A 105 (2008) 365-370
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 365-370
    • Nausch, L.W.M.1    Lecloux, J.2    Bonev, A.D.3    Nelson, M.T.4    Dostmann, W.R.5
  • 33
    • 59349118696 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter of ATP:ADP ratio
    • An interesting example of a single FP-based biosensor where cpmVenus was inserted at a certain position of GlnK1 protein. Depending on the ATP:ADP ratio, this biosensor showed different excitabilities at wavelengths 405 nm and 490 nm, therefore allowing for ratiometric measurement of ATP:ADP ratio by excitation. This study is also a good example of tuning and optimizing biosensors.
    • Berg J., Hung Y.P., and Yellen G. A genetically encoded fluorescent reporter of ATP:ADP ratio. Nat Methods 6 (2009) 161-166. An interesting example of a single FP-based biosensor where cpmVenus was inserted at a certain position of GlnK1 protein. Depending on the ATP:ADP ratio, this biosensor showed different excitabilities at wavelengths 405 nm and 490 nm, therefore allowing for ratiometric measurement of ATP:ADP ratio by excitation. This study is also a good example of tuning and optimizing biosensors.
    • (2009) Nat Methods , vol.6 , pp. 161-166
    • Berg, J.1    Hung, Y.P.2    Yellen, G.3
  • 34
    • 0030784698 scopus 로고    scopus 로고
    • Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson G.H., Knobel S.M., Sharif W.D., Kain S.R., and Piston D.W. Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys J 73 (1997) 2782-2790
    • (1997) Biophys J , vol.73 , pp. 2782-2790
    • Patterson, G.H.1    Knobel, S.M.2    Sharif, W.D.3    Kain, S.R.4    Piston, D.W.5
  • 35
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis J., McCaffery J.M., Miyawaki A., Farquhar M.G., and Tsien R.Y. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc Natl Acad Sci U S A 95 (1998) 6803-6808
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 36
    • 68949122860 scopus 로고    scopus 로고
    • Red fluorescent protein pH biosensor to detect concentrative nucleoside transport
    • Johnson D.E., Ai H.W., Wong P., Young J.D., Campbell R.E., and Casey J.R. Red fluorescent protein pH biosensor to detect concentrative nucleoside transport. J Biol Chem 284 (2009) 20499-20511
    • (2009) J Biol Chem , vol.284 , pp. 20499-20511
    • Johnson, D.E.1    Ai, H.W.2    Wong, P.3    Young, J.D.4    Campbell, R.E.5    Casey, J.R.6
  • 37
    • 44849091515 scopus 로고    scopus 로고
    • Application of fluorescence lifetime imaging of enhanced green fluorescent protein to intracellular pH measurements
    • An elegant example of utilizing FLIM to circumvent the disadvantages of intensiometric measurement. It also demonstrates how EGFP in lifetime measurements can be used for quantitative estimation of pH changes.
    • Nakabayashi T., Wang H.P., Kinjo M., and Ohta N. Application of fluorescence lifetime imaging of enhanced green fluorescent protein to intracellular pH measurements. Photochem Photobiol Sci 7 (2008) 668-670. An elegant example of utilizing FLIM to circumvent the disadvantages of intensiometric measurement. It also demonstrates how EGFP in lifetime measurements can be used for quantitative estimation of pH changes.
    • (2008) Photochem Photobiol Sci , vol.7 , pp. 668-670
    • Nakabayashi, T.1    Wang, H.P.2    Kinjo, M.3    Ohta, N.4
  • 38
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenbock G., De Angelis D.A., and Rothman J.E. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394 (1998) 192-195
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 39
    • 61449216130 scopus 로고    scopus 로고
    • In vivo measurement of cytosolic and mitochondrial pH using a pH-sensitive GFP derivative in Saccharomyces cerevisiae reveals a relation between intracellular pH and growth
    • Orij R., Postmus J., Ter Beek A., Brul S., and Smits G.J. In vivo measurement of cytosolic and mitochondrial pH using a pH-sensitive GFP derivative in Saccharomyces cerevisiae reveals a relation between intracellular pH and growth. Microbiology 155 (2009) 268-278
    • (2009) Microbiology , vol.155 , pp. 268-278
    • Orij, R.1    Postmus, J.2    Ter Beek, A.3    Brul, S.4    Smits, G.J.5
  • 40
    • 59849109401 scopus 로고    scopus 로고
    • Real-time measurement of endosomal acidification by a novel genetically encoded biosensor
    • Serresi M., Bizzarri R., Cardarelli F., and Beltram F. Real-time measurement of endosomal acidification by a novel genetically encoded biosensor. Anal Bioanal Chem 393 (2009) 1123-1133
    • (2009) Anal Bioanal Chem , vol.393 , pp. 1123-1133
    • Serresi, M.1    Bizzarri, R.2    Cardarelli, F.3    Beltram, F.4
  • 41
    • 59849109889 scopus 로고    scopus 로고
    • Green fluorescent protein based pH indicators for in vivo use: a review
    • Bizzarri R., Serresi M., Luin S., and Beltram F. Green fluorescent protein based pH indicators for in vivo use: a review. Anal Bioanal Chem 393 (2009) 1107-1122
    • (2009) Anal Bioanal Chem , vol.393 , pp. 1107-1122
    • Bizzarri, R.1    Serresi, M.2    Luin, S.3    Beltram, F.4
  • 42
    • 0842344106 scopus 로고    scopus 로고
    • Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators
    • Hanson G.T., Aggeler R., Oglesbee D., Cannon M., Capaldi R.A., Tsien R.Y., and Remington S.J. Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators. J Biol Chem 279 (2004) 13044-13053
    • (2004) J Biol Chem , vol.279 , pp. 13044-13053
    • Hanson, G.T.1    Aggeler, R.2    Oglesbee, D.3    Cannon, M.4    Capaldi, R.A.5    Tsien, R.Y.6    Remington, S.J.7
  • 44
    • 57449104199 scopus 로고    scopus 로고
    • pHlameleons: a family of FRET-based protein sensors for quantitative pH imaging
    • An interesting example of FRET-based pH biosensor that is composed of a pH-insensitive donor fluorophore and a pH-sensitive acceptor fluorophore. Unlike the conventional FRET-based biosensors that depend on the changes in relative distance and/or orientation of the fluorophores, this biosensor depends on the spectral changes of the acceptor fluorophore that accompany pH changes which in turn change the overlap integral affecting FRET.
    • Esposito A., Gralle M., Dani M.A.C., Lange D., and Wouters F.S. pHlameleons: a family of FRET-based protein sensors for quantitative pH imaging. Biochemistry 47 (2008) 13115-13126. An interesting example of FRET-based pH biosensor that is composed of a pH-insensitive donor fluorophore and a pH-sensitive acceptor fluorophore. Unlike the conventional FRET-based biosensors that depend on the changes in relative distance and/or orientation of the fluorophores, this biosensor depends on the spectral changes of the acceptor fluorophore that accompany pH changes which in turn change the overlap integral affecting FRET.
    • (2008) Biochemistry , vol.47 , pp. 13115-13126
    • Esposito, A.1    Gralle, M.2    Dani, M.A.C.3    Lange, D.4    Wouters, F.S.5
  • 45
    • 52549114763 scopus 로고    scopus 로고
    • A genetically encoded ratiometric sensor to measure extracellular pH in microdomains bounded by basolateral membranes of epithelial cells
    • Urra J., Sandoval M., Cornejo I., Barros L.F., Sepulveda F.V., and Cid L.P. A genetically encoded ratiometric sensor to measure extracellular pH in microdomains bounded by basolateral membranes of epithelial cells. Pflugers Arch 457 (2008) 233-242
    • (2008) Pflugers Arch , vol.457 , pp. 233-242
    • Urra, J.1    Sandoval, M.2    Cornejo, I.3    Barros, L.F.4    Sepulveda, F.V.5    Cid, L.P.6
  • 46
    • 42949146948 scopus 로고    scopus 로고
    • Fluorescent protein FRET pairs for ratiometric imaging of dual biosensors
    • An interesting example of detecting caspase-3 activity in the cytoplasm and nucleus using two orthogonal FRET pairs simultaneously. This study shows how the utilization of these FRET pairs preserved the temporal resolution of the caspase-3 activity in the cytoplasm and in the nucleus.
    • Ai H.W., Hazelwood K.L., Davidson M.W., and Campbell R.E. Fluorescent protein FRET pairs for ratiometric imaging of dual biosensors. Nat Methods 5 (2008) 401-403. An interesting example of detecting caspase-3 activity in the cytoplasm and nucleus using two orthogonal FRET pairs simultaneously. This study shows how the utilization of these FRET pairs preserved the temporal resolution of the caspase-3 activity in the cytoplasm and in the nucleus.
    • (2008) Nat Methods , vol.5 , pp. 401-403
    • Ai, H.W.1    Hazelwood, K.L.2    Davidson, M.W.3    Campbell, R.E.4
  • 47
    • 65449153321 scopus 로고    scopus 로고
    • Genetically encoded FRET-based biosensors for multiparameter fluorescence imaging
    • Carlson H.J., and Campbell R.E. Genetically encoded FRET-based biosensors for multiparameter fluorescence imaging. Curr Opin Biotechnol 20 (2009) 19-27
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 19-27
    • Carlson, H.J.1    Campbell, R.E.2


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